1F1J: Caspase-7

Crystal structure of caspase-7 in complex with acetyl-asp-glu-val-asp-cho. Determined by X-ray diffraction at 2.35 Å resolution. Released 23 May 2001.

Method: X-ray diffraction
Resolution: 2.35 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,164
Mol. weight: 70.27 kDa
Released: 23 May 2001

Explore 1F1J in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1F1J contains 18 α-helices and 40 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 9 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	59	1	1
β-strand	66-74	9	2
α-helix	84-86	3
α-helix	90-104	15
β-strand	106-112	7	2
α-helix	116-128	13
α-helix	131-133	3
β-strand	134-142	9	2
β-strand	145-146	2	3
β-strand	149-151	3	3
β-strand	156-158	3	3
α-helix	159-164	6
α-helix	172-174	3
β-strand	179-184	6	2
β-strand	190	1	4
β-strand	192	1	5
β-strand	195	1	6
β-strand	213	1	7
β-strand	219-223	5	2
β-strand	229	1	4
β-strand	232-234	3	8
β-strand	238-239	2	8
α-helix	240-252	13
α-helix	258-272	15
α-helix	280-282	3
β-strand	286	1	5
β-strand	290-293	4	2
β-strand	298	1	1

Chain B: 9 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	359	1	9
β-strand	366-374	9	2
α-helix	380-382	3
α-helix	390-404	15
β-strand	406-412	7	2
α-helix	416-428	13
β-strand	434-442	9	2
β-strand	445-446	2	10
β-strand	449-451	3	10
β-strand	456-458	3	10
α-helix	459-463	5
α-helix	464-466	3
α-helix	472-474	3
β-strand	479-484	6	2
β-strand	488-490	3	11
β-strand	492	1	12
β-strand	495	1	7
β-strand	513	1	6
β-strand	519-523	5	2
β-strand	528-529	2	11
β-strand	532-534	3	13
β-strand	538-539	2	13
α-helix	540-552	13
α-helix	558-572	15
α-helix	580-582	3
β-strand	586	1	12
β-strand	590-593	4	2
β-strand	598	1	9

Chain C: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	703-704	2	8

Chain D: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	803-804	2	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Caspase-7 protease	A, B	protein	305	Homo sapiens	P55210 (AlphaFold model)
Ace-asp-glu-val-asp-cho	C, D	protein	5

Sequence of entity 1 (A, B), FASTA

>1F1J_1 CASPASE-7 PROTEASE (chains A, B)
MLEADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLFSKKKKNVTMRSIKTTRDRVPTY
QYNMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAK
MQDLLKKASEEDHTNAACFACILLSHGEENVIYGKDGVTPIKDLTAHFRGDRSKTLLEKP
KLFFIQACRGTELDDGIQADSGPINDTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRG
SWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESQSDDPHFHEKKQIPCVVSMLTKE
LYFSQ

Sequence of entity 2 (C, D), FASTA

>1F1J_2 ACE-ASP-GLU-VAL-ASP-CHO (chains C, D)
XDEVX

Primary citation

The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity. Wei, Y., Fox, T., Chambers, S.P. et al. Chem Biol (2000) 7:423-432. DOI 10.1016/S1074-5521(00)00123-X · PubMed

Other PDB entries of the same protein (UniProt P55210 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4JR2 1.65 Å, Human procaspase-7/caspase-7 heterodimer bound to Ac-DEVD-CMK
4JB8 1.7 Å, Caspase-7 in Complex with DARPin C7_16
2QL9 2.14 Å, Crystal Structure of Caspase-7 with inhibitor AC-DQMD-CHO
4JR1 2.15 Å, Human procaspase-7 bound to Ac-DEVD-CMK
5K20 2.2 Å, Caspase-7 S239E Phosphomimetic
2QLB 2.25 Å, Crystal Structure of caspase-7 with inhibitor AC-ESMD-CHO
4LSZ 2.26 Å, Caspase-7 in Complex with DARPin D7.18
4ZVR 2.3 Å, Caspase-7 Variant 4 (V4) with reprogrammed substrate specificity due to…
2QL5 2.34 Å, Crystal Structure of caspase-7 with inhibitor AC-DMQD-CHO
6CL2 2.35 Å, Caspase-7 in complex with Ac-ATS009-KE
1I4O 2.4 Å, Crystal structure of the xiap/caspase-7 complex
2QL7 2.4 Å, Crystal Structure of Caspase-7 with inhibitor AC-IEPD-CHO

Browse structure collections

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